2011
The zipcode-binding protein ZBP1 influences the subcellular location of the Ro 60-kDa autoantigen and the noncoding Y3 RNA
Sim S, Yao J, Weinberg DE, Niessen S, Yates JR, Wolin SL. The zipcode-binding protein ZBP1 influences the subcellular location of the Ro 60-kDa autoantigen and the noncoding Y3 RNA. RNA 2011, 18: 100-110. PMID: 22114317, PMCID: PMC3261732, DOI: 10.1261/rna.029207.111.Peer-Reviewed Original ResearchConceptsY3 RNASubcellular locationCRM1 inhibitor leptomycin B.RNA-binding proteinExport signalVertebrate nucleiVertebrate cellsY RNAsRNA bindingLeptomycin B.Nuclear exportSubcellular localizationNoncoding RNAsRNA complexZBP1Ro proteinCellular componentsRNACytoplasmProteinNucleusCRM1Complex increasesExportUV irradiation
2001
Phosphorylation of the Saccharomyces cerevisiae La protein does not appear to be required for its functions in tRNA maturation and nascent RNA stabilization.
Long K, Cedervall T, Walch-Solimena C, Noe D, Huddleston M, Annan R, Wolin S. Phosphorylation of the Saccharomyces cerevisiae La protein does not appear to be required for its functions in tRNA maturation and nascent RNA stabilization. RNA 2001, 7: 1589-602. PMID: 11720288, PMCID: PMC1370201.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAutoantigensBinding SitesCell NucleolusCell NucleusFungal ProteinsMolecular Sequence DataPeptide MappingPhosphorylationProtein IsoformsRibonucleoproteinsRibonucleoproteins, Small NuclearRNARNA StabilityRNA-Binding ProteinsRNA, FungalRNA, TransferSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsConceptsLa proteinAbundant nuclear phosphoproteinRNA polymerase III transcriptsS. cerevisiae proteinTwo-dimensional gel electrophoresisRole of phosphorylationPolymerase III transcriptsCerevisiae proteinsNascent RNANascent transcriptsS. pombeSchizosaccharomyces pombeLhp1pPhosphorylation sitesYeast SaccharomycesProtein functionMutant versionSubcellular locationFirst proteinHuman proteinsNuclear phosphoproteinExonucleolytic degradationSerine phosphorylationPhosphorylation statusRNA stabilization
2000
Ro ribonucleoproteins contribute to the resistance of Deinococcus radiodurans to ultraviolet irradiation
Chen X, Quinn A, Wolin S. Ro ribonucleoproteins contribute to the resistance of Deinococcus radiodurans to ultraviolet irradiation. Genes & Development 2000, 14: 777-782. PMID: 10766734, PMCID: PMC316496, DOI: 10.1101/gad.14.7.777.Peer-Reviewed Original Research
1999
Two Yeast La Motif-containing Proteins Are RNA-binding Proteins that Associate with Polyribosomes
Sobel S, Wolin S. Two Yeast La Motif-containing Proteins Are RNA-binding Proteins that Associate with Polyribosomes. Molecular Biology Of The Cell 1999, 10: 3849-3862. PMID: 10564276, PMCID: PMC25684, DOI: 10.1091/mbc.10.11.3849.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAutoantigensFungal ProteinsGene DeletionGene Expression Regulation, FungalMicrofilament ProteinsMolecular Sequence DataPhylogenyPolyribosomesProtein BiosynthesisProtein Synthesis InhibitorsRibonucleoproteinsRNA-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentConceptsRNA-binding proteinLa proteinRNA polymerase III transcriptsMotif-containing proteinsSaccharomyces cerevisiae proteinsPolymerase III transcriptsWild-type strainCerevisiae proteinsLa motifProtein synthesis inhibitorU6 RNASro9pIndirect immunofluorescence microscopyMRNA translationImmunofluorescence microscopyLhp1pEssential processProteinSynthesis inhibitorNormal pathwayDeletionMotifLHP1SLF1RibosomesSaccharomyces cerevisiae telomerase is an Sm small nuclear ribonucleoprotein particle
Seto A, Zaug A, Sobel S, Wolin S, Cech T. Saccharomyces cerevisiae telomerase is an Sm small nuclear ribonucleoprotein particle. Nature 1999, 401: 177-180. PMID: 10490028, DOI: 10.1038/43694.Peer-Reviewed Original ResearchConceptsSm proteinsSaccharomyces cerevisiae telomeraseNuclear messenger RNASmall nuclear ribonucleoprotein particleRNA polymerase IISmall nuclear ribonucleoproteinNuclear ribonucleoprotein particleTrimethylguanosine capPolymerase IIRNA processingTelomerase RNAEnzyme telomeraseNuclear ribonucleoproteinRibonucleoprotein particleProtein subunitsMessenger RNATelomeraseTelomerase activityRNAProteinEukaryotesSnRNPsYeast extractRibonucleoproteinChromosomesThe trials and travels of tRNA
Wolin S, Matera A. The trials and travels of tRNA. Genes & Development 1999, 13: 1-10. PMID: 9887094, DOI: 10.1101/gad.13.1.1.Peer-Reviewed Original Research
1998
A role for the yeast La protein in U6 snRNP assembly: evidence that the La protein is a molecular chaperone for RNA polymerase III transcripts
Pannone B, Xue D, Wolin S. A role for the yeast La protein in U6 snRNP assembly: evidence that the La protein is a molecular chaperone for RNA polymerase III transcripts. The EMBO Journal 1998, 17: 7442-7453. PMID: 9857199, PMCID: PMC1171088, DOI: 10.1093/emboj/17.24.7442.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAutoantigensFungal ProteinsGene DosageMolecular ChaperonesMolecular Sequence DataMutationN-Terminal Acetyltransferase CRibonucleoprotein, U4-U6 Small NuclearRibonucleoproteinsRibonucleoproteins, Small NuclearRNA Polymerase IIIRNA PrecursorsRNA-Binding ProteinsRNA, FungalRNA, MessengerSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidSnRNP Core ProteinsConceptsU6 snRNP assemblyPolymerase III transcriptsRNA polymerase III transcriptsSnRNP assemblyU6 snRNPLa proteinMolecular chaperonesYeast La proteinSm-like proteinsCore Sm proteinsFamily of proteinsSm proteinsU5 snRNPsU6 RNALhp1pFirst proteinPolymerase IIILa autoantigenNovel componentYeast cellsSnRNPEarly stepsLsm8pProteinTranscriptsBinding of the 60-kDa Ro autoantigen to Y RNAs: evidence for recognition in the major groove of a conserved helix.
Green C, Long K, Shi H, Wolin S. Binding of the 60-kDa Ro autoantigen to Y RNAs: evidence for recognition in the major groove of a conserved helix. RNA 1998, 4: 750-65. PMID: 9671049, PMCID: PMC1369656, DOI: 10.1017/s1355838298971667.Peer-Reviewed Original ResearchConceptsY RNAsSpecific base pairsRo proteinRRNA precursorConserved helixMajor grooveBase pairsSmall cytoplasmic RNAThree-nucleotide bulgeProtein side chainsProtein bindsCytoplasmic RNARNA sequencesProtein recognitionRNAXenopus oocytesProteinHelixRo autoantigenDistinct classesDiethyl pyrocarbonateProtein bindingStructural alterationsSide chainsDimethyl sulfate
1997
The La protein in Schizosaccharomyces pombe: a conserved yet dispensable phosphoprotein that functions in tRNA maturation.
Van Horn D, Yoo C, Xue D, Shi H, Wolin S. The La protein in Schizosaccharomyces pombe: a conserved yet dispensable phosphoprotein that functions in tRNA maturation. RNA 1997, 3: 1434-43. PMID: 9404894, PMCID: PMC1369584.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAutoantigensCarrier ProteinsCytoskeletal ProteinsFungal ProteinsHumansMolecular Sequence DataPhosphoproteinsPhosphorylationRecombinant Fusion ProteinsRestriction MappingRibonucleoproteinsRNA Processing, Post-TranscriptionalRNA-Binding ProteinsRNA, FungalRNA, TransferSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSchizosaccharomycesSequence Homology, Amino AcidConceptsLa proteinAbundant nuclear phosphoproteinRNA polymerase III transcriptsFission yeast SchizosaccharomycesPre-tRNA maturationS. pombe cellsPolymerase III transcriptsWild-type cellsHuman La proteinYeast SchizosaccharomycesS. pombePombe cellsYeast SaccharomycesTRNA precursorsNuclear phosphoproteinPattern of tRNAS. cerevisiaeLa autoantigenTRNAProteinSchizosaccharomycesPhosphoproteinYeastExhibit alterationsMaturationThe Yeast La Protein Is Required for the 3′ Endonucleolytic Cleavage That Matures tRNA Precursors
Yoo C, Wolin S. The Yeast La Protein Is Required for the 3′ Endonucleolytic Cleavage That Matures tRNA Precursors. Cell 1997, 89: 393-402. PMID: 9150139, DOI: 10.1016/s0092-8674(00)80220-2.Peer-Reviewed Original ResearchMeSH KeywordsAutoantigensBase CompositionCell DivisionEndonucleasesExonucleasesFungal ProteinsGene Expression Regulation, EnzymologicGene Expression Regulation, FungalMolecular Sequence DataMutationNucleic Acid ConformationRibonucleoproteinsRNA PrecursorsRNA-Binding ProteinsRNA, Transfer, SerSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription FactorsConceptsTrailer sequencesEndonucleolytic cleavageLa autoantigen bindsYeast La proteinPolymerase III transcriptsS. cerevisiae cellsEndonucleolytic removalLhp1pTRNA precursorsLa proteinCerevisiae cellsAnticodon stemSecond mutationMutationsCellsCleavageTranscriptsProteinBindsSequenceMaturationStemConformation
1996
A misfolded form of 5S rRNA is complexed with the Ro and La autoantigens.
Shi H, O'Brien C, Van Horn D, Wolin S. A misfolded form of 5S rRNA is complexed with the Ro and La autoantigens. RNA 1996, 2: 769-84. PMID: 8752087, PMCID: PMC1369414.Peer-Reviewed Original ResearchConceptsRRNA precursorRo proteinAlternative helixQuality control pathwaysYeast Saccharomyces cerevisiaeSmall cytoplasmic RNAProtein-protein interactionsOligonucleotide-directed RNase H cleavageWild-type precursorRRNA biosynthesisY RNAsSecondary structure determinantsMutant RNAsSaccharomyces cerevisiaeLa proteinControl pathwaysCytoplasmic RNANuclease digestionInternal mutationsRRNARNAXenopus oocytesProteinSimilar sequencesRo autoantigen
1995
Caenorhabditis elegans embryos contain only one major species of Ro RNP.
Van Horn D, Eisenberg D, O'Brien C, Wolin S. Caenorhabditis elegans embryos contain only one major species of Ro RNP. RNA 1995, 1: 293-303. PMID: 7489501, PMCID: PMC1369082.Peer-Reviewed Original ResearchConceptsY RNAsRo proteinRo RNPsC. elegans proteinsRNA recognition motifHuman Y RNAsN-terminal extensionPyrimidine-rich internal loopRo autoantigenRNP functionVertebrate proteinsDiscard pathwayVertebrate cellsC. elegansInvertebrate speciesNematode CaenorhabditisVertebrate speciesProtein functionHuman proteinsRNA biosynthesisDefective precursorsRecognition motifRNA moleculesGenetic analysisRNA
1994
A possible role for the 60-kD Ro autoantigen in a discard pathway for defective 5S rRNA precursors.
O'Brien C, Wolin S. A possible role for the 60-kD Ro autoantigen in a discard pathway for defective 5S rRNA precursors. Genes & Development 1994, 8: 2891-2903. PMID: 7995526, DOI: 10.1101/gad.8.23.2891.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAutoantibodiesAutoantigensAutoimmune DiseasesBase SequenceDNA PrimersDNA, ComplementaryFemaleHumansMolecular Sequence DataMolecular WeightMutagenesisNucleic Acid ConformationOocytesOvaryPolymerase Chain ReactionRibonucleoproteinsRNA PrecursorsRNA, Ribosomal, 5SRNA, Small CytoplasmicTranscription, GeneticXenopusConceptsDiscard pathwayRRNA precursorCytoplasmic RNA-protein complexesRNA-protein complexesVariety of vertebratesRo autoantigenRo RNPsRRNA productionProtein bindsMutant RNAsRRNA sequencesMore point mutationsAdditional nucleotidesRo proteinRRNAPoint mutationsTerminal extensionXenopus oocytesProteinRNAPathwayPossible roleVertebratesRNPsNucleotidesLa proteins from Drosophila melanogaster and Saccharomyces cerevisiae: a yeast homolog of the La autoantigen is dispensable for growth.
Yoo C, Wolin S. La proteins from Drosophila melanogaster and Saccharomyces cerevisiae: a yeast homolog of the La autoantigen is dispensable for growth. Molecular And Cellular Biology 1994, 14: 5412-5424. PMID: 8035818, PMCID: PMC359060, DOI: 10.1128/mcb.14.8.5412.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAutoantigensBase SequenceChromosome MappingCloning, MolecularDNA PrimersDrosophila melanogasterFungal ProteinsGenes, FungalGenes, InsectMolecular Sequence DataMutagenesis, InsertionalNuclear ProteinsPlant ProteinsRibonucleoproteinsRNA Polymerase IIIRNA-Binding ProteinsRNA, Ribosomal, 5SSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentSequence Homology, Amino AcidConceptsLa proteinDrosophila melanogasterYeast La proteinRNA polymerase IIIPolymerase III transcriptsHuman La proteinYeast homologTranscription extractProtein homologsYeast proteinsVertebrate speciesYeast SaccharomycesProtein functionRedundant rolesHuman proteinsPolymerase IIISaccharomyces cerevisiaeLa autoantigenNull allelesGenetic analysisYeast cellsDrosophilaAutoantigen LaHomologBiochemical properties
1993
Xenopus Ro ribonucleoproteins: members of an evolutionarily conserved class of cytoplasmic ribonucleoproteins.
O'Brien C, Margelot K, Wolin S. Xenopus Ro ribonucleoproteins: members of an evolutionarily conserved class of cytoplasmic ribonucleoproteins. Proceedings Of The National Academy Of Sciences Of The United States Of America 1993, 90: 7250-7254. PMID: 7688474, PMCID: PMC47114, DOI: 10.1073/pnas.90.15.7250.Peer-Reviewed Original ResearchConceptsY RNAsRo proteinSmall ribonucleoproteinHuman Y RNAsSmall RNA moleculesXenopus egg extractsAmino acid sequenceY-RNAsHY3 RNAsVertebrate speciesMammalian cellsRo RNPsSubcellular locationRNA componentCytoplasmic ribonucleoproteinHY5 RNAAdditional proteinsRNA moleculesAcid sequenceHuman RNAEgg extractsEntire proteinConserved stemOocyte cytoplasmRibonucleoprotein
1987
A Subset of Yeast snRNA's Contains Functional Binding Sites for the Highly Conserved Sm Antigen
Riedel N, Wolin S, Guthrie C. A Subset of Yeast snRNA's Contains Functional Binding Sites for the Highly Conserved Sm Antigen. Science 1987, 235: 328-331. PMID: 2948278, DOI: 10.1126/science.2948278.Peer-Reviewed Original Research
1983
Genes for two small cytoplasmic Ro RNAs are adjacent and appear to be single-copy in the human genome
Wolin S, Steitz J. Genes for two small cytoplasmic Ro RNAs are adjacent and appear to be single-copy in the human genome. Cell 1983, 32: 735-744. PMID: 6187471, DOI: 10.1016/0092-8674(83)90059-4.Peer-Reviewed Original ResearchConceptsHuman genomeRo RNAsSecondary structure homologyRNA polymerase IIISmall cytoplasmic ribonucleoproteinsClass III genesGenomic clonesMammalian cellsPolymerase IIIRNA componentStructure homologySingle copyCytoplasmic ribonucleoproteinHY5 RNAMouse cellsHuman cellsHY1Cell extractsGenesRNAGenomeRNAsHY3CellsMY1